ID   LPXB_RHOPB              Reviewed;         396 AA.
AC   Q215D6;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Lipid-A-disaccharide synthase {ECO:0000255|HAMAP-Rule:MF_00392};
DE            EC=2.4.1.182 {ECO:0000255|HAMAP-Rule:MF_00392};
GN   Name=lpxB {ECO:0000255|HAMAP-Rule:MF_00392}; OrderedLocusNames=RPC_2449;
OS   Rhodopseudomonas palustris (strain BisB18).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316056;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB18;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Condensation of UDP-2,3-diacylglucosamine and 2,3-
CC       diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor
CC       of lipid A, a phosphorylated glycolipid that anchors the
CC       lipopolysaccharide to the outer membrane of the cell.
CC       {ECO:0000255|HAMAP-Rule:MF_00392}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-
CC         glucosamine = a lipid A disaccharide + H(+) + UDP;
CC         Xref=Rhea:RHEA:67828, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:137748, ChEBI:CHEBI:176338, ChEBI:CHEBI:176343;
CC         EC=2.4.1.182; Evidence={ECO:0000255|HAMAP-Rule:MF_00392};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00392}.
CC   -!- SIMILARITY: Belongs to the LpxB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00392}.
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DR   EMBL; CP000301; ABD88000.1; -; Genomic_DNA.
DR   RefSeq; WP_011472897.1; NC_007925.1.
DR   AlphaFoldDB; Q215D6; -.
DR   SMR; Q215D6; -.
DR   STRING; 316056.RPC_2449; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   PRIDE; Q215D6; -.
DR   EnsemblBacteria; ABD88000; ABD88000; RPC_2449.
DR   KEGG; rpc:RPC_2449; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_0_5; -.
DR   OMA; PTVWAWR; -.
DR   OrthoDB; 1258510at2; -.
DR   UniPathway; UPA00973; -.
DR   GO; GO:0008915; F:lipid-A-disaccharide synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00392; LpxB; 1.
DR   InterPro; IPR003835; Glyco_trans_19.
DR   PANTHER; PTHR30372; PTHR30372; 1.
DR   Pfam; PF02684; LpxB; 1.
DR   TIGRFAMs; TIGR00215; lpxB; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Transferase.
FT   CHAIN           1..396
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000255215"
SQ   SEQUENCE   396 AA;  43002 MW;  1301C262E03031FB CRC64;
     MTAVATHAVR KIFLIATEES GDRLGASLMR ELRDRLGAAV RFEGVGGRAM AREGLTSLFP
     IEELSIIGLS AVARRLPTIL RHIRTAAHAA LQAAPDVLVI IDSPDFTHRV ARRVRARDPS
     IPIVNYVSPT VWAWRPGRAK VMRKYVDHVL ALLPFEPDEY RRLQGPPCSY VGHPLTEQIA
     TLRPNPEEQL RRDAAPPVLL VLPGSRRSEI RHHMAVFGEA LGLLQAQGVA FELILPTMPH
     LEALIAEALK HWPLQPRVVV GENDKRAAFR IARAALAKSG TVTLELAVAG VPMVTAYRAG
     QLEAWIVRRR ITSASVILAN LVVGENVAPE YLQEECTAPT LAAALRDVLA DSPLRQRQLA
     AFGRIDAIMS TGAQSPSACA ADIVLGLLPA AAPALR